1E8F
STRUCTURE OF THE H61T MUTANT OF THE FLAVOENZYME VANILLYL-ALCOHOL OXIDASE IN THE APO FORM
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004458 | molecular_function | D-lactate dehydrogenase (cytochrome) activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005777 | cellular_component | peroxisome |
A | 0008720 | molecular_function | D-lactate dehydrogenase activity |
A | 0015945 | biological_process | methanol metabolic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0018465 | molecular_function | vanillyl-alcohol oxidase activity |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
A | 0071949 | molecular_function | FAD binding |
A | 1903457 | biological_process | lactate catabolic process |
B | 0003824 | molecular_function | catalytic activity |
B | 0004458 | molecular_function | D-lactate dehydrogenase (cytochrome) activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005739 | cellular_component | mitochondrion |
B | 0005777 | cellular_component | peroxisome |
B | 0008720 | molecular_function | D-lactate dehydrogenase activity |
B | 0015945 | biological_process | methanol metabolic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0018465 | molecular_function | vanillyl-alcohol oxidase activity |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0071949 | molecular_function | FAD binding |
B | 1903457 | biological_process | lactate catabolic process |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | ACT_SITE: |
Chain | Residue | Details |
A | TYR108 | |
A | TYR503 | |
A | ARG504 | |
B | TYR108 | |
B | TYR503 | |
B | ARG504 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | SITE: Important for the catalytic mechanism; Involved in substrate deprotonation |
Chain | Residue | Details |
A | ASP170 | |
B | ASP170 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Tele-8alpha-FAD histidine |
Chain | Residue | Details |
A | HIS422 | |
B | HIS422 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1vao |
Chain | Residue | Details |
A | ARG504 | |
A | HIS422 | |
A | TYR503 | |
A | ASP170 | |
A | TYR108 |
site_id | CSA2 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1vao |
Chain | Residue | Details |
B | ARG504 | |
B | HIS422 | |
B | TYR503 | |
B | ASP170 | |
B | TYR108 |
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 103 |
Chain | Residue | Details |
A | TYR108 | electrostatic stabiliser, hydrogen bond donor |
A | ASP170 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
A | HIS422 | activator, covalently attached, increase redox potential |
A | TYR503 | electrostatic stabiliser, hydrogen bond donor |
A | ARG504 | activator, electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA2 |
Number of Residues | 5 |
Details | M-CSA 103 |
Chain | Residue | Details |
B | TYR108 | electrostatic stabiliser, hydrogen bond donor |
B | ASP170 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
B | HIS422 | activator, covalently attached, increase redox potential |
B | TYR503 | electrostatic stabiliser, hydrogen bond donor |
B | ARG504 | activator, electrostatic stabiliser, hydrogen bond donor |